2DDE
Structure of cinnamycin complexed with lysophosphatidylethanolamine
Summary for 2DDE
| Entry DOI | 10.2210/pdb2dde/pdb |
| Related | 1AJ1 1MQX 1MQY 1MQZ 1QOW 1W9N 1WCO 2KTN 2KTO |
| Related PRD ID | PRD_000195 |
| Descriptor | LANTIBIOTIC CINNAMYCIN, (7S)-4,7-DIHYDROXY-10-OXO-3,5,9-TRIOXA-4-PHOSPHAUNDECAN-1-AMINIUM 4-OXIDE (2 entities in total) |
| Functional Keywords | antibiotic, immunopotentiator, antimicrobial, antitumor, lipid binding, phosphatidylethanolamine, lanthionine, thioester |
| Biological source | STREPTOMYCES GRISEOVERTICILLATUS |
| Total number of polymer chains | 1 |
| Total formula weight | 2325.56 |
| Authors | Hosoda, K.,Ohya, M.,Kohno, T.,Maeda, T.,Endo, S.,Wakamatsu, K. (deposition date: 2006-01-27, release date: 2006-02-21, Last modification date: 2024-07-10) |
| Primary citation | Hosoda, K.,Ohya, M.,Kohno, T.,Maeda, T.,Endo, S.,Wakamatsu, K. Structure determination of an immunopotentiator peptide, cinnamycin, complexed with lysophosphatidylethanolamine by 1H-NMR1. J.Biochem., 119:226-230, 1996 Cited by PubMed Abstract: The three-dimensional structure of a complex of cinnamycin, a 19-amino acid residue immunopotentiator peptide, and lysophosphatidylethanolamine was determined by 1H-NMR. The complex was cylindrical in shape, 11 A in diameter and 26 A in length, excluding the acyl chain of the phospholipid. The peptide had a hydrophobic pocket surrounded by residues Phe-7 through Ala(S)-14 to bind to the head group of the ligand. Fitting of the head group to the hydrophobic pocket was so good that other than a glycerophosphoethanolamine head group would be unable to fit the pocket. The goodness of the fitting is compatible with the strict specificity of ligand binding of the peptide. PubMed: 8882709DOI: 10.1093/oxfordjournals.jbchem.a021226 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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